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Database: UniProt
Entry: A0A100I8R5_ASPNG
LinkDB: A0A100I8R5_ASPNG
Original site: A0A100I8R5_ASPNG 
ID   A0A100I8R5_ASPNG        Unreviewed;       770 AA.
AC   A0A100I8R5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Choline kinase {ECO:0000313|EMBL:GAQ36280.1};
GN   ORFNames=ABL_01586 {ECO:0000313|EMBL:GAQ36280.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36280.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC       {ECO:0000256|ARBA:ARBA00038211}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ36280.1}.
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DR   EMBL; BCMY01000002; GAQ36280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100I8R5; -.
DR   VEuPathDB; FungiDB:An01g11150; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1102057; -.
DR   VEuPathDB; FungiDB:ATCC64974_14550; -.
DR   VEuPathDB; FungiDB:M747DRAFT_242474; -.
DR   OMA; CEQVINW; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05157; ETNK_euk; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR007521; Choline_kin_N.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR   PANTHER; PTHR22603:SF93; RE24176P; 1.
DR   Pfam; PF04428; Choline_kin_N; 1.
DR   Pfam; PF01633; Choline_kinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:GAQ36280.1};
KW   Transferase {ECO:0000313|EMBL:GAQ36280.1}.
FT   DOMAIN          208..281
FT                   /note="Choline kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04428"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  86071 MW;  D576448BC7D48B40 CRC64;
     MPSVTDQTGL SGLEFDGPQP ILGTGLNVSP QRHHHTNGHE SSAIGSEGNA FRHRVPAPKK
     SAARLPTHQP ASLSSQTSSV ITEPAHRLEK DGMSKNGEED PQNSLFAQVY EWLQREKSKR
     RSHKATNLAA MDGVASDGDD DDDDGASVLV ERPLSSGADA AMALDKLEKI LIQYATSRQG
     TDSVHFARRS GRRRQYSKGL RRGSASESDF SDHEAAAPSV DAVLDNSKTL AYSGGGGTED
     DDNENSVSAR RAKDKEAWAL FKSEILRLTH TMQLKGWRKL PMELAADIGV VRLSGALTNA
     VYVVTPPQNI PVPKAEDGSY SLVPRKPPPK LLLRIYGPQV DHLIDRDNEL QILRRLGRKN
     IGPKVLGIFN NGRFEEYFEA RPLTPKELRD PPTMKQIAKR MRELHDGIDL LVDEREGGPM
     VFNNWDKWVD RCEQVINWLD KEIRSEHNKS KAASEAWRRR GFVCGVPWPF FRKAVEGYRK
     WLLSSCGGME GIKRQLVFAH NDTQYGNLLR MEPSHESPLL RPENVHKQLV VIDFEYASAN
     TPGIEFANHF TEWCYNYHDA ERPWACDTSR YPNPEQQHQF IEAYLSHRPG LREQASPSIT
     PLMRGLSTNT SSLAPLNLDD GPDVDVSSRF DIEKAHEDST SAKIQFYARQ TRLWRVLNSA
     QWVAWGIVQA KVPGMEEGIA ADEAAAKAQN GHHGTNGNGV HSDVTAEVNH STGTPPVDAD
     VDEAEEFDYL AYAQDRAMFF WSDLLALKII REDELPESLV QVIKARMIDY
//
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